Deoxyhypusine synthase: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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-<StructureSection load='2emt' size='340' side='right' caption='Mouse radixin FERM domain (green) complex with N-terminal peptide of the adhesion molecule PSGL-1 (yellow) (PDB code [[2emt]])' scene='77/777076/Cv/1'>
+<StructureSection load='6xxk' size='340' side='right' caption='Human deoxypusine synthase with mercaptocysteine complex with spermidine, ethylene glycol, formate, acetate,  mercaptoethanol, MPD (PDB code [[6xxk]])' scene='87/874448/Cv/7'>
 == Function ==
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 == Disease ==
-Mutations in DHS result in reduced enzyme activity that limits the hypusination of elf5A which is associated with neurodevelopmental disorder<ref>PMID:30661771</ref>.
+Mutations in DHS result in reduced enzyme activity that limit the hypusination of elf5A which is associated with neurodevelopmental disorder<ref>PMID:30661771</ref>.
 ==Relevance ==
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 == Structural highlights ==
-The <scene name='77/777076/Cv/3'>hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule</scene> hydrophobic groove of the FERM domain of Rdx binds the N-terminal peptide of the adhesion molecule P-selectin glycoprotein ligand 1 with multiple hydrogen bonds<ref>PMID:18706570</ref>. {{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}
+The Biological assembly of Human deoxypusine synthase is <scene name='87/874448/Cv/6'>homotetramer</scene> (PDB code [[6xxk]]). <scene name='87/874448/Cv/5'>The complex between DHS and its substrate spermidine</scene> shows the binding in the active site with spermidine forming hydrogen bonds to DHS with its 2 terminal amino groups <ref>PMID:32235505</ref>. Water molecules are shown as red spheres.
 </StructureSection>
 == 3D Structures of deoxyhypusine synthase ==